Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a common set of genes with diverse functions

Estelle Nicolas, Gyu Lee Min, Mohamed Ali Hakimi, Hugh P. Cam, Shiv I S Grewal, Ramin Shiekhattar

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

Schizosaccharomyces pombe contains two proteins, SWIRM1 and SWIRM2, with close homology to human histone H3 lysine 4 demethylase. Both proteins contain the amino oxidase catalytic domain and a recently described DNA interaction SWIRM domain. Here we describe the biochemical isolation and the functional characterization of SWIRM1 and SWIRM2. Our results indicate that while SWIRM2 is an essential gene, cells lacking SWIRM1 are viable. We found that SWIRM1 and SWIRM2 are stably associated in a multiprotein complex, but intriguingly, unlike their human counterpart, S. pombe SWIRM complex contains neither a histone deacetylase nor any detectable demethylase activity. Genome-wide chromatin immunoprecipitation unexpectedly showed the absence of both SWIRM proteins from heterochromatic domains. Instead, consistent with biochemical analyses, SWIRM1 and SWIRM2 co-localize to a common set of target gene promoters whose functions are implicated in diverse processes including mitochondrial metabolism and transcriptional regulation. Importantly, we show that SWIRM1 is not only required for optimum transcription of its target genes but also display a global role in regulation of antisense transcription.

Original languageEnglish (US)
Pages (from-to)35983-35988
Number of pages6
JournalJournal of Biological Chemistry
Volume281
Issue number47
DOIs
StatePublished - Nov 24 2006
Externally publishedYes

Fingerprint

Schizosaccharomyces
Histones
Yeast
Lysine
Genes
Multiprotein Complexes
Histone Deacetylases
Chromatin Immunoprecipitation
Essential Genes
Transcription
Catalytic Domain
Oxidoreductases
Proteins
Genome
DNA
Metabolism
Chromatin
Protein Domains

ASJC Scopus subject areas

  • Biochemistry

Cite this

Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a common set of genes with diverse functions. / Nicolas, Estelle; Min, Gyu Lee; Hakimi, Mohamed Ali; Cam, Hugh P.; Grewal, Shiv I S; Shiekhattar, Ramin.

In: Journal of Biological Chemistry, Vol. 281, No. 47, 24.11.2006, p. 35983-35988.

Research output: Contribution to journalArticle

Nicolas, Estelle ; Min, Gyu Lee ; Hakimi, Mohamed Ali ; Cam, Hugh P. ; Grewal, Shiv I S ; Shiekhattar, Ramin. / Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a common set of genes with diverse functions. In: Journal of Biological Chemistry. 2006 ; Vol. 281, No. 47. pp. 35983-35988.
@article{ace104085978420ca1fa65428c823a20,
title = "Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a common set of genes with diverse functions",
abstract = "Schizosaccharomyces pombe contains two proteins, SWIRM1 and SWIRM2, with close homology to human histone H3 lysine 4 demethylase. Both proteins contain the amino oxidase catalytic domain and a recently described DNA interaction SWIRM domain. Here we describe the biochemical isolation and the functional characterization of SWIRM1 and SWIRM2. Our results indicate that while SWIRM2 is an essential gene, cells lacking SWIRM1 are viable. We found that SWIRM1 and SWIRM2 are stably associated in a multiprotein complex, but intriguingly, unlike their human counterpart, S. pombe SWIRM complex contains neither a histone deacetylase nor any detectable demethylase activity. Genome-wide chromatin immunoprecipitation unexpectedly showed the absence of both SWIRM proteins from heterochromatic domains. Instead, consistent with biochemical analyses, SWIRM1 and SWIRM2 co-localize to a common set of target gene promoters whose functions are implicated in diverse processes including mitochondrial metabolism and transcriptional regulation. Importantly, we show that SWIRM1 is not only required for optimum transcription of its target genes but also display a global role in regulation of antisense transcription.",
author = "Estelle Nicolas and Min, {Gyu Lee} and Hakimi, {Mohamed Ali} and Cam, {Hugh P.} and Grewal, {Shiv I S} and Ramin Shiekhattar",
year = "2006",
month = "11",
day = "24",
doi = "10.1074/jbc.M606349200",
language = "English (US)",
volume = "281",
pages = "35983--35988",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "47",

}

TY - JOUR

T1 - Fission yeast homologs of human histone H3 lysine 4 demethylase regulate a common set of genes with diverse functions

AU - Nicolas, Estelle

AU - Min, Gyu Lee

AU - Hakimi, Mohamed Ali

AU - Cam, Hugh P.

AU - Grewal, Shiv I S

AU - Shiekhattar, Ramin

PY - 2006/11/24

Y1 - 2006/11/24

N2 - Schizosaccharomyces pombe contains two proteins, SWIRM1 and SWIRM2, with close homology to human histone H3 lysine 4 demethylase. Both proteins contain the amino oxidase catalytic domain and a recently described DNA interaction SWIRM domain. Here we describe the biochemical isolation and the functional characterization of SWIRM1 and SWIRM2. Our results indicate that while SWIRM2 is an essential gene, cells lacking SWIRM1 are viable. We found that SWIRM1 and SWIRM2 are stably associated in a multiprotein complex, but intriguingly, unlike their human counterpart, S. pombe SWIRM complex contains neither a histone deacetylase nor any detectable demethylase activity. Genome-wide chromatin immunoprecipitation unexpectedly showed the absence of both SWIRM proteins from heterochromatic domains. Instead, consistent with biochemical analyses, SWIRM1 and SWIRM2 co-localize to a common set of target gene promoters whose functions are implicated in diverse processes including mitochondrial metabolism and transcriptional regulation. Importantly, we show that SWIRM1 is not only required for optimum transcription of its target genes but also display a global role in regulation of antisense transcription.

AB - Schizosaccharomyces pombe contains two proteins, SWIRM1 and SWIRM2, with close homology to human histone H3 lysine 4 demethylase. Both proteins contain the amino oxidase catalytic domain and a recently described DNA interaction SWIRM domain. Here we describe the biochemical isolation and the functional characterization of SWIRM1 and SWIRM2. Our results indicate that while SWIRM2 is an essential gene, cells lacking SWIRM1 are viable. We found that SWIRM1 and SWIRM2 are stably associated in a multiprotein complex, but intriguingly, unlike their human counterpart, S. pombe SWIRM complex contains neither a histone deacetylase nor any detectable demethylase activity. Genome-wide chromatin immunoprecipitation unexpectedly showed the absence of both SWIRM proteins from heterochromatic domains. Instead, consistent with biochemical analyses, SWIRM1 and SWIRM2 co-localize to a common set of target gene promoters whose functions are implicated in diverse processes including mitochondrial metabolism and transcriptional regulation. Importantly, we show that SWIRM1 is not only required for optimum transcription of its target genes but also display a global role in regulation of antisense transcription.

UR - http://www.scopus.com/inward/record.url?scp=33845994062&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33845994062&partnerID=8YFLogxK

U2 - 10.1074/jbc.M606349200

DO - 10.1074/jbc.M606349200

M3 - Article

C2 - 16990277

AN - SCOPUS:33845994062

VL - 281

SP - 35983

EP - 35988

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 47

ER -